The
presence of cavities and tunnels in the interior of proteins, in
conjunction with the structural plasticity arising from the coupling to
the thermal fluctuations of the protein scaffold, has profound
consequences on the pathways followed by ligands moving through the
protein matrix. Through an integrated approach using quantitative
analysis of experimental rebinding kinetics from laser flash
photolysis, trapping of unstable conformational states by embedding
proteins within the nanopores of silica gels, and molecular simulations
we try to gain insight into the migration mechanism of ligands.

The
development of genetically encoded photoswitchable fluorescent proteins
is of greatest interest to expand the toolkit of fluorescent reporters
suitable for super-resolution microscopy applications based on random activation of single molecules.We are
exploiting YtvA, a photochromicblue light photoreceptor from Bacillus
subtilis, as a fluorescent probe for superresolution microscopy.
Current efforst include novel GAF domains.

We
exploit proteins as nanosized carriers for photosensitizers. The
nanostructured materials are inherently theranostic devices, with built
in terapeutic (photosensitized production of singlet oxygen) and
diagnostic (through their fluorescence emission) capabilities.